ID   CPSF2_XENLA             Reviewed;         783 AA.
AC   Q9W799;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 2;
DE   AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE            Short=CPSF 100 kDa subunit;
GN   Name=cpsf2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10409759; DOI=10.1128/mcb.19.8.5707;
RA   Dickson K.S., Bilger A., Ballantyne S., Wickens M.P.;
RT   "The cleavage and polyadenylation specificity factor in Xenopus laevis
RT   oocytes is a cytoplasmic factor involved in regulated polyadenylation.";
RL   Mol. Cell. Biol. 19:5707-5717(1999).
RN   [2]
RP   IDENTIFICATION IN A COMPLEX WITH CPSF2, CPSF73, CPSF160 AND SYMPK, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12006661; DOI=10.1091/mbc.01-12-0567;
RA   Hofmann I., Schnoelzer M., Kaufmann I., Franke W.W.;
RT   "Symplekin, a constitutive protein of karyo- and cytoplasmic particles
RT   involved in mRNA biogenesis in Xenopus laevis oocytes.";
RL   Mol. Biol. Cell 13:1665-1676(2002).
RN   [3]
RP   INTERACTION WITH SYMPK.
RX   PubMed=15550246; DOI=10.1016/j.cell.2004.10.029;
RA   Barnard D.C., Ryan K., Manley J.L., Richter J.D.;
RT   "Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic
RT   polyadenylation.";
RL   Cell 119:641-651(2004).
CC   -!- FUNCTION: CPSF plays a key role in pre-mRNA 3'-end formation,
CC       recognizing the AAUAAA signal sequence and interacting with poly(A)
CC       polymerase and other factors to bring about cleavage and poly(A)
CC       addition. In X.laevis this subunit seems to be predominantly involved
CC       in cytoplasmic polyadenylation reaction. May also be involved in the
CC       histone 3'-end pre-mRNA processing.
CC   -!- SUBUNIT: CPSF is a heterotetramer composed of four distinct subunits
CC       160, 100, 70 and 30 kDa (By similarity). Identification in a complex
CC       with cpsf2, cpsf73, cpsf160 and sympk. Interacts with sympk.
CC       {ECO:0000250, ECO:0000269|PubMed:12006661,
CC       ECO:0000269|PubMed:15550246}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000269|PubMed:12006661}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF139986; AAD33061.1; -; mRNA.
DR   RefSeq; NP_001081123.1; NM_001087654.1.
DR   AlphaFoldDB; Q9W799; -.
DR   SMR; Q9W799; -.
DR   BioGRID; 98996; 1.
DR   IntAct; Q9W799; 1.
DR   GeneID; 394394; -.
DR   KEGG; xla:394394; -.
DR   CTD; 394394; -.
DR   Xenbase; XB-GENE-950598; cpsf2.S.
DR   OrthoDB; 1314980at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 394394; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR022712; Beta_Casp.
DR   InterPro; IPR027075; CPSF2.
DR   InterPro; IPR025069; Cpsf2_C.
DR   InterPro; IPR035639; CPSF2_MBL.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   PANTHER; PTHR45922; PTHR45922; 1.
DR   Pfam; PF10996; Beta-Casp; 1.
DR   Pfam; PF13299; CPSF100_C; 1.
DR   Pfam; PF16661; Lactamase_B_6; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   SMART; SM01027; Beta-Casp; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..783
FT                   /note="Cleavage and polyadenylation specificity factor
FT                   subunit 2"
FT                   /id="PRO_0000074395"
FT   REGION          407..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  88986 MW;  F68558C78CF0AEDC CRC64;
     MTSIIKLTTL VGAQEESAVC YLLQVDEFRF LLDCGWDENF SMDIIDSVKK YVHQVDAVLL
     SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FSLFSLDDVD
     CAFDKIQQLK YNQIVHLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR
     EIHLNGCSLE MINRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA
     GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
     NPFQFRHLTL CHGYSDLARV PSPKVVLASQ PDLECGFSRE LFIQWCQDPK NSVILTYRTT
     PGTLARFLID HPSERIIDIE LRKRVKLEGK ELEEYVEKEK LKKEAAKKLE QSKEADLDSS
     DDSDVEEDID QITSHKAKHD LMMKNEGSRK GSFFKQAKKS YPMFPAPEDR IKWDEYGEII
     KPEDFLVPEL QVTEDEKTKL ESGLTNGDEP MDQDLSDVPT KCVSTTESME IKARVTYIDY
     EGRSDGDSIK KIINQMKPRQ LIIVHGPPDA TQDLAEACRA FGGKDIKVYT PKLHETVDAT
     SETHIYQVRL KDSLVSSLKF CKAKDTELAW IDGVLDMRVS KVDTGVILEE RELKDEGEDM
     EMQVDTQVMD ASTIAQQKVI KSLFGDDDKE FSEESEIIPT LEPLPSNEVP GHQSVFMNEP
     RLSDFKQVLL REGIHAEFVG GVLVCNNMVA VRRTETGRIG LEGCLCEDFF KIRELLYEQY
     AIV